X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (29133) 29133
Newsletter (6901) 6901
Publication (3026) 3026
Book Review (2893) 2893
Book Chapter (308) 308
Dissertation (85) 85
Conference Proceeding (82) 82
Newspaper Article (31) 31
Government Document (18) 18
Reference (16) 16
Book / eBook (15) 15
Magazine Article (9) 9
Web Resource (3) 3
Data Set (2) 2
Journal / eJournal (2) 2
Paper (1) 1
Trade Publication Article (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (24601) 24601
animals (13184) 13184
cysteine (12182) 12182
humans (12101) 12101
proteases (9634) 9634
biochemistry & molecular biology (9337) 9337
research (6543) 6543
apoptosis (6121) 6121
cysteine endopeptidases - metabolism (5343) 5343
proteins (5308) 5308
amino acid sequence (4948) 4948
cystine (4909) 4909
cysteine proteinases (4794) 4794
molecular sequence data (4699) 4699
mice (4445) 4445
analysis (3873) 3873
cell biology (3830) 3830
universities and colleges (3795) 3795
reports (3606) 3606
enzymes (3494) 3494
thiols (3461) 3461
expression (3363) 3363
cysteine proteinase inhibitors - pharmacology (3239) 3239
male (2754) 2754
female (2544) 2544
cysteine protease (2536) 2536
rats (2527) 2527
cancer (2354) 2354
physiological aspects (2308) 2308
cysteine endopeptidases - genetics (2252) 2252
activation (2148) 2148
biophysics (2070) 2070
immunology (2069) 2069
gene expression (1998) 1998
cell line (1988) 1988
biochemistry (1960) 1960
kinetics (1915) 1915
oxidative stress (1898) 1898
models, molecular (1880) 1880
protease (1858) 1858
protein binding (1816) 1816
identification (1815) 1815
cathepsins (1813) 1813
peptides (1812) 1812
cells, cultured (1807) 1807
cells (1803) 1803
proteolysis (1782) 1782
proteasome endopeptidase complex (1773) 1773
article (1754) 1754
cysteine endopeptidases - chemistry (1733) 1733
cysteine proteases (1729) 1729
microbiology (1725) 1725
protease inhibitors (1703) 1703
multidisciplinary sciences (1649) 1649
base sequence (1634) 1634
binding sites (1620) 1620
substrate specificity (1606) 1606
apoptosis - drug effects (1592) 1592
cysteine proteinase (1560) 1560
mutation (1519) 1519
protein (1465) 1465
purification (1440) 1440
amino acids (1412) 1412
research article (1408) 1408
in-vitro (1350) 1350
genetic aspects (1339) 1339
pharmacology & pharmacy (1315) 1315
cysteine endopeptidases (1307) 1307
cell research (1284) 1284
oncology (1281) 1281
health aspects (1277) 1277
genes (1273) 1273
signal transduction (1273) 1273
parasitology (1251) 1251
multienzyme complexes - metabolism (1239) 1239
protein conformation (1239) 1239
inhibition (1231) 1231
degradation (1227) 1227
cysteine - metabolism (1219) 1219
inhibitors (1200) 1200
protease inhibitors - pharmacology (1198) 1198
sequence homology, amino acid (1183) 1183
cell line, tumor (1182) 1182
neurosciences (1180) 1180
cloning, molecular (1171) 1171
cathepsin l (1160) 1160
crystal-structure (1160) 1160
papain (1149) 1149
cysteine - chemistry (1141) 1141
protein structure, tertiary (1139) 1139
enzyme activation (1137) 1137
blotting, western (1134) 1134
biology (1121) 1121
structure-activity relationship (1119) 1119
plant sciences (1113) 1113
gene (1110) 1110
chemistry, medicinal (1106) 1106
recombinant proteins - metabolism (1105) 1105
hydrogen-ion concentration (1098) 1098
sequence alignment (1082) 1082
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (36087) 36087
Chinese (67) 67
Japanese (58) 58
German (32) 32
Russian (29) 29
Spanish (25) 25
French (20) 20
Polish (10) 10
Korean (9) 9
Portuguese (8) 8
Czech (6) 6
Italian (4) 4
Ukrainian (3) 3
Arabic (1) 1
Hungarian (1) 1
Persian (1) 1
Romanian (1) 1
Swedish (1) 1
Turkish (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Journal Article
2011, Advances in experimental medicine and biology, ISBN 9781441984135, Volume 712., xix, 226
Cysteine proteases expressed by pathogenic organisms play key roles in virulence including host entry, feeding and suppression of host immune responses. This... 
chemistry | Cysteine proteinases | Cysteine Proteases | Microbial enzymes | Pathogenic microorganisms | Eukaryota | Pathophysiology | Bacteria | Viruses | immunology | enzymology | Pre-clinical Medicine: Basic Sciences | Molecular Medicine | Biomedicine general | Biomedicine
Book
The Plant Cell, ISSN 1040-4651, 8/2008, Volume 20, Issue 8, pp. 2252 - 2264
Bacterial wilt, a disease impacting cultivated crops worldwide, is caused by the pathogenic bacterium Ralstonia solanacearum. PopP2 (for Pseudomonas outer... 
Proteins | Disease resistance | Pathogens | Receptors | Ralstonia solanacearum | Genes | Fluorescence | Plants | Vacuoles | Plant cells | LIFETIME IMAGING MICROSCOPY | FOR-GENE CONCEPT | BIOCHEMISTRY & MOLECULAR BIOLOGY | III EFFECTOR | AGROBACTERIUM-MEDIATED TRANSFORMATION | CLADOSPORIUM-FULVUM | PLANT INNATE IMMUNITY | PLANT SCIENCES | CELL BIOLOGY | PROGRAMMED CELL-DEATH | TOMATO LYCOPERSICON-ESCULENTUM | HYPERSENSITIVE RESPONSE | CF-2-DEPENDENT DISEASE RESISTANCE | Arabidopsis Proteins - genetics | Arabidopsis Proteins - physiology | Plants, Genetically Modified - genetics | Plant Diseases - microbiology | Reverse Transcriptase Polymerase Chain Reaction | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Arabidopsis - microbiology | Gene Expression Regulation, Plant - drug effects | Cell Nucleus - metabolism | Cysteine Endopeptidases - metabolism | Plants, Genetically Modified - metabolism | Plants, Genetically Modified - microbiology | Cysteine Endopeptidases - genetics | Ralstonia solanacearum - metabolism | Bacterial Proteins - metabolism | Plant Diseases - genetics | Ralstonia solanacearum - genetics | Microscopy, Fluorescence | Arabidopsis thaliana | Infection | Cysteine | Proteases | Cystine | Protein binding | Index Medicus | programmed cell-death | hypersensitive respon | plant innate immunity | for-gene concept | lifetime imaging microscopy | tomato lycopersicon-esculentum | agrobacterium-mediated transformation | cf-2-dependent disease resistance | iii effector | cladosporium-fulvum
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2015, Volume 290, Issue 32, pp. 19403 - 19422
All coronaviruses, including the recently emerged Middle East respiratory syndrome coronavirus (MERS-CoV) from the beta-CoV subgroup, require the proteolytic... 
DIMER INTERFACE | DESIGN | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOLOGICAL EVALUATION | MAIN PROTEASE | DIFFRACTION DATA | INHIBITORS | CATALYTIC-ACTIVITY | 3C-LIKE PROTEASE | SARS-CORONAVIRUS | Cysteine Endopeptidases - chemistry | Peptidomimetics - chemical synthesis | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Viral Proteins - metabolism | Cysteine Endopeptidases - metabolism | Antiviral Agents - chemistry | Escherichia coli - metabolism | Middle East Respiratory Syndrome Coronavirus - enzymology | Recombinant Proteins - metabolism | Amino Acid Sequence | Antiviral Agents - pharmacology | Gene Expression | Peptidomimetics - pharmacology | Viral Proteins - chemistry | Middle East Respiratory Syndrome Coronavirus - drug effects | Recombinant Proteins - chemistry | Viral Proteins - genetics | Viral Proteins - antagonists & inhibitors | Peptidomimetics - chemistry | Recombinant Proteins - genetics | Sequence Alignment | Escherichia coli - genetics | Middle East Respiratory Syndrome Coronavirus - genetics | Cysteine Endopeptidases - genetics | Antiviral Agents - chemical synthesis | Hydrophobic and Hydrophilic Interactions | Ligands | Molecular Docking Simulation | Kinetics | Protein Multimerization - drug effects | Index Medicus | viral protease | X-ray crystallography | Protein Structure and Folding | analytical ultracentrifugation | monomer-dimer equilibrium | enzyme inhibitor | ligand-induced dimerization | β-CoV | enzyme inactivation | MERS-CoV 3CLpro | enzyme kinetics
Journal Article
1998, 2nd ed., Protein profile, ISBN 0198502494, 131
Book
FEBS Letters, ISSN 0014-5793, 08/1991, Volume 288, Issue 1-2, pp. 201 - 205
A computer‐assisted comparative analysis of the amino acid sequences of (putative) thiol proteases encoded by the genomes of several diverse groups or... 
Papain-like protease | Catalytic center | Sequence motif | RNA virus | Polyprotein processing | Semliki forest virus | CPI and CP2 | cylindrical inclusion (potyvirus protein) | Ross River virus | TEV | Actinidia chinensis actinidin | ‘Streptococcus-like’ protease | VEEV | MidV | TVMV | SPL | major mite fecal allergen | SH-EP | rubella virus (rubivirus) | calpain | avian bronchitis virus (coronaviruses) | SPP | PVY | RRV | MHV | potato virus Y | barley yellow mosaic virus (bymovirus) | cathepsin B | Homo sapiens | cathepsins H and L | Sindbis virus | actin | murine hepatitis virus | Middelburg virus (alphaviruses) | plum pox virus | aleur | Cat.H and L | Vigna mungo | FMDV A10 | Ananas comosus | Mus musculus | ONNV | papain and omega | Rattus norvegicus | cysteine endopeptidase | Venezuelan equine encephalomyelitis virus | SNBV | calp | BaYMV | Dictyostelium discoideum | RuV | Cat.B | PPV | Streptococcus pyogenes | Carica papaya | IBV | aleurain | bromelain | peptidase A | bromel | SFV | cysteine proteinase 1 and 2 | tobacco vein mottling virus (potyviruses) | Hordeum vulgare | derpt | helper component | L-pro | Dermatophagoides pteronyssinus | O'Nyong-Nyong virus | tobacco etch virus | proteinase I and III, respectively | ‘leader’, or accessory protease (see text) | foot-and-mouth-disease virus A10 strain (aphthovirus) | M-pro | ‘main’ protease | Cysteine Endopeptidases - chemistry | Amino Acid Sequence | Aphthovirus - enzymology | Plant Viruses - enzymology | Sequence Alignment | Alphavirus - enzymology | RNA Viruses - enzymology | Molecular Sequence Data | Protein Sorting Signals - chemistry | Rubella virus - enzymology | Coronaviridae - enzymology | Papain - chemistry | RNA viruses | papain | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2001, Volume 276, Issue 5, pp. 3149 - 3157
Journal Article
The New Phytologist, ISSN 0028-646X, 7/2010, Volume 187, Issue 2, pp. 313 - 331
Senescence is the highly regulated last developmental phase of plant organs and tissues, and is optimized to allow nutrient remobilization to surviving plant... 
Leaves | Barley | Genes | Chlorides | Cellular senescence | Amino acids | Nitrates | Plants | Nitrogen | Nutrient solutions | C : N ratio | family C1A cysteine protease | Hordeum vulgare | family S10 serine carboxypeptidase | barley | nitrogen remobilization | protein degradation | leaf senescence | Protein degradation | C: N ratio | Family C1A cysteine protease | Nitrogen remobilization | Hordeum vulgare (barley) | Leaf senescence | Family S10 serine carboxypeptidase | C:N ratio | RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE | ARABIDOPSIS-THALIANA | SUGARS | PLANT SCIENCES | TOBACCO-LEAVES | L. LEAVES | SENESCING LEAVES | CHLOROPLAST PROTEINS | DEGRADATION | PLANTS | METABOLIC-REGULATION | Solubility - drug effects | Carbohydrate Metabolism - drug effects | Ribulose-Bisphosphate Carboxylase - genetics | Carbohydrate Metabolism - genetics | Cellular Senescence - drug effects | Hordeum - enzymology | Photosynthesis - genetics | Protein Processing, Post-Translational - drug effects | Enzyme Induction - drug effects | Nitrogen - pharmacology | Plant Leaves - drug effects | Plant Proteins - metabolism | Plant Leaves - enzymology | Cysteine Proteases - biosynthesis | Multigene Family - genetics | Cellular Senescence - genetics | Nitrogen - metabolism | Reverse Transcriptase Polymerase Chain Reaction | Nitrates - metabolism | Plant Proteins - genetics | Ribulose-Bisphosphate Carboxylase - metabolism | Gene Expression Regulation, Plant - drug effects | Plant Leaves - genetics | Photosynthesis - drug effects | Hydroponics | Hordeum - growth & development | Hordeum - genetics | Cysteine | Metabolites | Proteases | Proteolysis | Phytochemistry | Genetic research | Gene expression | Photosynthesis | Cystine | Index Medicus | Indexing in process
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 8/2000, Volume 150, Issue 4, pp. 887 - 894
Calpains and caspases are two cysteine protease families that play important roles in regulating pathological cell death. Here, we report that m-calpain may be... 
Oxygen | Calcium | Cell death |